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| | <StructureSection load='5c4i' size='340' side='right'caption='[[5c4i]], [[Resolution|resolution]] 2.27Å' scene=''> | | <StructureSection load='5c4i' size='340' side='right'caption='[[5c4i]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c4i]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] and [http://en.wikipedia.org/wiki/Moorella_thermoacetica_(strain_atcc_39073) Moorella thermoacetica (strain atcc 39073)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C4I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c4i]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica_ATCC_39073 Moorella thermoacetica ATCC 39073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C4I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxalate_oxidoreductase Oxalate oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.10 1.2.7.10] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c4i OCA], [https://pdbe.org/5c4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c4i RCSB], [https://www.ebi.ac.uk/pdbsum/5c4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c4i ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c4i OCA], [http://pdbe.org/5c4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c4i RCSB], [http://www.ebi.ac.uk/pdbsum/5c4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c4i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OORA_MOOTA OORA_MOOTA]] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.<ref>PMID:20956531</ref> [[http://www.uniprot.org/uniprot/OORB_MOOTA OORB_MOOTA]] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.<ref>PMID:20956531</ref> [[http://www.uniprot.org/uniprot/OORD_MOOTA OORD_MOOTA]] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.<ref>PMID:20956531</ref> | + | [https://www.uniprot.org/uniprot/OORA_MOOTA OORA_MOOTA] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.<ref>PMID:20956531</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Moorella thermoacetica]] | + | [[Category: Moorella thermoacetica ATCC 39073]] |
| - | [[Category: Oxalate oxidoreductase]]
| + | [[Category: Brignole EJ]] |
| - | [[Category: Brignole, E J]] | + | [[Category: Can M]] |
| - | [[Category: Can, M]] | + | [[Category: Drennan CL]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Gibson MI]] |
| - | [[Category: Gibson, M I]] | + | [[Category: Pierce E]] |
| - | [[Category: Pierce, E]] | + | [[Category: Ragsdale SW]] |
| - | [[Category: Ragsdale, S W]] | + | |
| - | [[Category: Ofor]]
| + | |
| - | [[Category: Oxalate]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Thiamine]]
| + | |
| Structural highlights
Function
OORA_MOOTA Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.[1]
Publication Abstract from PubMed
Thiamine pyrophosphate (TPP), a derivative of vitamin B1, is a versatile and ubiquitous cofactor. When coupled with [4Fe-4S] clusters in microbial 2-oxoacid:ferredoxin oxidoreductases (OFORs), TPP is involved in catalyzing low-potential redox reactions that are important for the synthesis of key metabolites and the reduction of N2, H+, and CO2. We have determined the high-resolution (2.27 A) crystal structure of the TPP-dependent oxalate oxidoreductase (OOR), an enzyme that allows microbes to grow on oxalate, a widely occurring dicarboxylic acid that is found in soil and freshwater and is responsible for kidney stone disease in humans. OOR catalyzes the anaerobic oxidation of oxalate, harvesting the low-potential electrons for use in anaerobic reduction and fixation of CO2. We compare the OOR structure to that of the only other structurally characterized OFOR family member, pyruvate:ferredoxin oxidoreductase. This side-by-side structural analysis highlights the key similarities and differences that are relevant for the chemistry of this entire class of TPP-utilizing enzymes.
The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism.,Gibson MI, Brignole EJ, Pierce E, Can M, Ragsdale SW, Drennan CL Biochemistry. 2015 Jun 24. PMID:26061898[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pierce E, Becker DF, Ragsdale SW. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. J Biol Chem. 2010 Dec 24;285(52):40515-24. doi: 10.1074/jbc.M110.155739. Epub, 2010 Oct 18. PMID:20956531 doi:http://dx.doi.org/10.1074/jbc.M110.155739
- ↑ Gibson MI, Brignole EJ, Pierce E, Can M, Ragsdale SW, Drennan CL. The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 2015 Jun 24. PMID:26061898 doi:http://dx.doi.org/10.1021/acs.biochem.5b00521
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